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Microb Cell Fact. 2019 Dec 23;18(1):216. doi: 10.1186/s12934-019-1270-2.

Soluble versions of outer membrane cytochromes function as exporters for heterologously produced cargo proteins.

Author information

1
Department of Molecular Microbiology and Bioenergetics, Goethe University, Frankfurt, Germany.
2
Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
3
Institute for Biological Interfaces, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany.
4
Department of Applied Biology, Institute for Applied Biosciences, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany. johannes.gescher@kit.edu.
5
Institute for Biological Interfaces, Karlsruhe Institute of Technology (KIT), Eggenstein-Leopoldshafen, Germany. johannes.gescher@kit.edu.

Abstract

This study reveals that it is possible to secrete truncated versions of outer membrane cytochromes into the culture supernatant and that these proteins can provide a basis for the export of heterologously produced proteins. Different soluble and truncated versions of the outer membrane cytochrome MtrF were analyzed for their suitability to be secreted. A protein version with a very short truncation of the N-terminus to remove the recognition sequence for the addition of a lipid anchor is secreted efficiently to the culture supernatant, and moreover this protein could be further truncated by a deletion of 160 amino acid and still is detectable in the supernatant. By coupling a cellulase to this soluble outer membrane cytochrome, the export efficiency was measured by means of relative cellulase activity. We conclude that outer membrane cytochromes of S. oneidensis can be applied as transporters for the export of target proteins into the medium using the type II secretion pathway.

KEYWORDS:

Cellulase; Fusion proteins; Outer membrane cytochromes; Protein export; Shewanella oneidensis; Type II secretion system

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